Open AccessLocalization of DING proteins on P st S ‐containing outer‐surface appendages of P seudomonas aeruginosa
Author(s) -
Shah Megha,
Zaborin Alexander,
Alverdy John C.,
Scott Ken,
Zaborina Olga
Publication year - 2014
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12368
Subject(s) - appendage , pseudomonas aeruginosa , biology , bacteria , plasmid , microbiology and biotechnology , bacterial outer membrane , extracellular , pseudomonas , phosphate , chemistry , biochemistry , gene , genetics , escherichia coli , anatomy
Phosphate signaling and acquisition are critical for the bacterial response to phosphate limitation, and bacteria express multiple factors to scavenge phosphate. We previously found that multidrug‐resistant strains of P seudomonas aeruginosa from critically ill patients can form unusual outer‐surface appendages harboring P st S proteins. Here, we have expanded our investigation to DING proteins that like P st S belong to the family of high‐affinity phosphate‐binding proteins but have strong similarity with eukaryotic DING proteins. We demonstrate the localization of DING on P st S ‐containing outer‐surface appendages in both multidrug‐resistant strain MDR 25 and the PA 14 strain of P . aeruginosa . However, the number of cells producing appendages and the amount of appendages on each cell in PA 14 were found to be negligible, unless overexpression of either P st S or DING was achieved by transformation with constructed plasmids. We further noticed that DING expression under low phosphate conditions was significantly higher in MDR25 compared to PA14 which may explain the greater abundance of appendages in MDR25. Our finding that DING proteins are localized on extracellular appendages provides an opportunity to study the interaction of bacterial DING with host proteins by mimicking the action of host DING s.